ID   GST_NOTSL               Reviewed;         203 AA.
AC   P46088;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 107.
DE   RecName: Full=Glutathione S-transferase;
DE            EC=2.5.1.18;
DE   AltName: Full=GST class-sigma;
OS   Nototodarus sloanii (Wellington flying squid) (Ommastrephes sloanei).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Cephalopoda;
OC   Coleoidea; Decapodiformes; Teuthida; Oegopsina; Ommastrephidae;
OC   Nototodarus.
OX   NCBI_TaxID=215440;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 33-60 AND
RP   86-104.
RC   STRAIN=Pacificus; TISSUE=Digestive gland;
RX   PubMed=8440736; DOI=10.1016/s0021-9258(18)53643-7;
RA   Tomarev S.I., Zinovieva R.D., Guo K., Piatigorsky J.;
RT   "Squid glutathione S-transferase. Relationships with other glutathione S-
RT   transferases and S-crystallins of cephalopods.";
RL   J. Biol. Chem. 268:4534-4542(1993).
RN   [2]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG,
RP   CATALYTIC ACTIVITY, FUNCTION, AND SUBUNIT.
RX   PubMed=7727393; DOI=10.1021/bi00016a003;
RA   Ji X., von Rosenvinge E.C., Johnson W.W., Tomarev S.I., Piatigorsky J.,
RA   Armstrong R.N., Gilliland G.L.;
RT   "Three-dimensional structure, catalytic properties, and evolution of a
RT   sigma class glutathione transferase from squid, a progenitor of the lens S-
RT   crystallins of cephalopods.";
RL   Biochemistry 34:5317-5328(1995).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE ANALOG.
RX   PubMed=8710848; DOI=10.1073/pnas.93.16.8208;
RA   Ji X., von Rosenvinge E.C., Johnson W.W., Armstrong R.N., Gilliland G.L.;
RT   "Location of a potential transport binding site in a sigma class
RT   glutathione transferase by X-ray crystallography.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:8208-8213(1996).
CC   -!- FUNCTION: High activity toward 1-chloro-2,4-dinitrobenzene. Not very
CC       efficient at catalyzing the addition of GSH to enones and epoxides.
CC       {ECO:0000269|PubMed:7727393}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutathione + RX = a halide anion + an S-substituted
CC         glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925,
CC         ChEBI:CHEBI:90779; EC=2.5.1.18;
CC         Evidence={ECO:0000269|PubMed:7727393};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:7727393,
CC       ECO:0000269|PubMed:8710848}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- TISSUE SPECIFICITY: More abundant in the digestive gland than in the
CC       testis, mantle, or lens.
CC   -!- SIMILARITY: Belongs to the GST superfamily. Sigma family.
CC       {ECO:0000305}.
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DR   EMBL; L02054; AAA92066.1; -; Genomic_DNA.
DR   EMBL; L02053; AAA92066.1; JOINED; Genomic_DNA.
DR   EMBL; L02052; AAA92066.1; JOINED; Genomic_DNA.
DR   EMBL; L02051; AAA92066.1; JOINED; Genomic_DNA.
DR   EMBL; L02050; AAA92066.1; JOINED; Genomic_DNA.
DR   PIR; A45463; A45463.
DR   PDB; 1GSQ; X-ray; 2.40 A; A=2-203.
DR   PDB; 2GSQ; X-ray; 2.20 A; A=2-203.
DR   PDBsum; 1GSQ; -.
DR   PDBsum; 2GSQ; -.
DR   AlphaFoldDB; P46088; -.
DR   SMR; P46088; -.
DR   EvolutionaryTrace; P46088; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004364; F:glutathione transferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006749; P:glutathione metabolic process; IEA:InterPro.
DR   InterPro; IPR010987; Glutathione-S-Trfase_C-like.
DR   InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR   InterPro; IPR040079; Glutathione_S-Trfase.
DR   InterPro; IPR004045; Glutathione_S-Trfase_N.
DR   InterPro; IPR004046; GST_C.
DR   InterPro; IPR003083; S-crystallin.
DR   InterPro; IPR036249; Thioredoxin-like_sf.
DR   Pfam; PF14497; GST_C_3; 1.
DR   Pfam; PF02798; GST_N; 1.
DR   PRINTS; PR01269; SCRYSTALLIN.
DR   SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR   SUPFAM; SSF47616; SSF47616; 1.
DR   SUPFAM; SSF52833; SSF52833; 1.
DR   PROSITE; PS50405; GST_CTER; 1.
DR   PROSITE; PS50404; GST_NTER; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Transferase.
FT   CHAIN           1..203
FT                   /note="Glutathione S-transferase"
FT                   /id="PRO_0000185920"
FT   DOMAIN          2..79
FT                   /note="GST N-terminal"
FT   DOMAIN          81..203
FT                   /note="GST C-terminal"
FT   BINDING         8
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:8710848"
FT   BINDING         39
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:7727393,
FT                   ECO:0000305|PubMed:8710848"
FT   BINDING         43
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:7727393,
FT                   ECO:0000305|PubMed:8710848"
FT   BINDING         49..51
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:7727393,
FT                   ECO:0000305|PubMed:8710848"
FT   BINDING         63..64
FT                   /ligand="glutathione"
FT                   /ligand_id="ChEBI:CHEBI:57925"
FT                   /evidence="ECO:0000305|PubMed:7727393,
FT                   ECO:0000305|PubMed:8710848"
FT   VARIANT         124
FT                   /note="C -> Y"
FT   MUTAGEN         107
FT                   /note="F->Y: Improves action on epones and epoxides."
FT   STRAND          4..8
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   STRAND          10..12
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           13..15
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           16..24
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   STRAND          30..33
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   TURN            36..38
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           39..42
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           43..45
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           47..49
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   STRAND          53..56
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   STRAND          59..61
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           64..74
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           82..106
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           113..136
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   TURN            137..140
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   STRAND          141..143
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           152..167
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   TURN            169..174
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           176..186
FT                   /evidence="ECO:0007829|PDB:2GSQ"
FT   HELIX           189..197
FT                   /evidence="ECO:0007829|PDB:2GSQ"
SQ   SEQUENCE   203 AA;  22919 MW;  F46F56682F1C9591 CRC64;
     MPKYTLHYFP LMGRAELCRF VLAAHGEEFT DRVVEMADWP NLKATMYSNA MPVLDIDGTK
     MSQSMCIARH LAREFGLDGK TSLEKYRVDE ITETLQDIFN DVVKIKFAPE AAKEAVQQNY
     EKSCKRLAPF LEGLLVSNGG GDGFFVGNSM TLADLHCYVA LEVPLKHTPE LLKDCPKIVA
     LRKRVAECPK IAAYLKKRPV RDF